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G7163

Sigma-Aldrich

α-Galactosidase, positionally specific from Escherichia coli

recombinant, expressed in E. coli, buffered aqueous solution

Synonym(s):

1,6-alpha-D-galactoside galactohydrolase, alpha-Galactosidase, melibiase

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32

recombinant

expressed in E. coli

Quality Level

form

buffered aqueous solution

specific activity

≥20 units/mg protein

mol wt

80 kDa

shipped in

wet ice

storage temp.

2-8°C

Gene Information

Escherichia coli CFT073 ... melA(1037886)

Biochem/physiol Actions

Cleaves α(1→3)- and α(1→6)-linked, non-reducing terminal galactose from complex carbohydrates and glycoproteins. It is particularly efficient for removing α-linked galactose under conditions where the pH must be neutral or above, for example, with live cells.

Unit Definition

One unit will hydrolyze 1 μmole of p-nitrophenyl α-D-galactopyranoside per min at pH 6.5 at 25 °C.

Physical form

This product is a sterile-filtered aqueous buffered solution.

inhibitor

Product No.
Description
Pricing

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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K Schmid et al.
European journal of biochemistry, 67(1), 95-104 (1976-08-01)
The utilization by Escherichia coli K12 of raffinose as sole carbon source depends on a new raffinose transport system, an invertase and an alpha-galactosidase specified by the Raf-plasmid D1021. The alpha-galactosidase was purified to homogeneity from a mutant strain with
Shuo Gao et al.
Frontiers in chemistry, 9, 709581-709581 (2021-08-03)
For wide applications of the lacZ gene in cellular/molecular biology, small animal investigations, and clinical assessments, the improvement of noninvasive imaging approaches to precisely assay gene expression has garnered much attention. In this study, we investigate a novel molecular platform
K Wyatt et al.
Health technology assessment (Winchester, England), 16(39), 1-543 (2012-10-24)
To determine natural history and estimate effectiveness and cost of enzyme replacement therapy (ERT) and substrate replacement therapy (SRT) for patients with Gaucher disease, Fabry disease, mucopolysaccharidosis type I (MPS I), mucopolysaccharidosis type II (MPS II), Pompe disease and Niemann-Pick
Delayed anaphylactic reaction to mammalian meat.
K Sekiya et al.
Journal of investigational allergology & clinical immunology, 22(6), 446-447 (2012-10-30)
Takura Wakinaka et al.
Glycobiology, 23(2), 232-240 (2012-10-24)
Bifidobacterium bifidum is one of the most frequently found bifidobacteria in the intestines of newborn infants. We previously reported that B. bifidum possesses unique metabolic pathways for O-linked glycans on gastrointestinal mucin (Yoshida E, Sakurama H, Kiyohara M, Nakajima M

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